ID   Q8CHM5_MOUSE            Unreviewed;       708 AA.
AC   Q8CHM5;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Ribosomal protein S6 kinase {ECO:0000313|EMBL:AAN71007.1};
DE   Flags: Fragment;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAN71007.1};
RN   [1] {ECO:0000313|EMBL:AAN71007.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ {ECO:0000313|EMBL:AAN71007.1};
RA   Brathwaite M., Waeltz P., Dudekula D., Qian Y., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic Sequence Analysis in the Mouse T-complex Region.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009804}.
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DR   EMBL; AF551762; AAN71007.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8CHM5; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05582; STKc_RSK_N; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR041906; RSK_N.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF213; RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000606-
KW   51}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAN71007.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000606-51};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Ribonucleoprotein {ECO:0000313|EMBL:AAN71007.1};
KW   Ribosomal protein {ECO:0000313|EMBL:AAN71007.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          286..355
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          382..647
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   ACT_SITE        507
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   BINDING         32..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         388..396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAN71007.1"
SQ   SEQUENCE   708 AA;  79908 MW;  156CDD42B331307E CRC64;
     EEGIVKEIDI SNHVKEGFEK ADPSQFELLK VLGQGSYGKV FLVRKVTGSD AGQLYAMKVL
     KKATLKVRDR VRSKMERDIL AEVNHPFIVK LHYAFQTEGK LYLILDFLRG GDLFTRLSKE
     VMFTEEDVKF YLAELALALD HLHGLGIIYR DLKPENILLD EEGHIKITDF GLSKEATDHD
     KRAYSFCGTI EYMAPEVVNR RGHTQSADWW SFGVLMFEML TGSLPFQGKD RKETMALILK
     AKLGMPQFLS AEAQSLLRAL FKRNPCNRLG AGVDGVEEIK RHPFFVTIDW NKLYRKEIKP
     PFKPAVGRPE DTFHFDPEFT ARTPTDSPGV PPSANAHHLF RGFSFVASSL VQEPSQQDVP
     KAPIHPIVQQ LHGNNIHFTD GYEIKEDIGV GSYSVCKRCV HKATDAEYAV KIIDKSKRDP
     SEEIEILLRY GQHPNIITLK DVYDDGKYVY LVMELMRGGE LLDRILRQRC FSEREASDVL
     YTIARTMDYL HSQGVGLPAL PVVVHRDLKP SNILYMDESG NPESIRICDF GFAKQLRAEN
     GLLMTPCYTA NFVAPEVLKR QGYDAACDVW SLGILLYTML AGFTPFANGP DDTPEEILAR
     IGSGKYALSG GNWDSISDAA KDVVSKMLHV DPQQRLTAVQ VLKHPWIVNR EYLSQNQLSR
     QDVHLVKGAM AATYFALNRT PQAPRLEPVL SSSLAQRRGM KRLTSTRL
//